3e20

Crystal structure of S.pombe eRF1/eRF3 complex

Method: X-RAY DIFFRACTION

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Eukaryotic peptide chain release factor GTP-binding subunit

Schizosaccharomyces pombe

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Eukaryotic peptide chain release factor subunit 1 × 1 （P79063）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Eukaryotic peptide chain release factor subunit 1 × 1 （P79063）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Eukaryotic peptide chain release factor subunit 1 × 1 （P79063）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Eukaryotic peptide chain release factor subunit 1 × 1 （P79063）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ERF3_SCHPO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–201； UniProt 467–662 Author chain D； PDBConstruct 6–201； UniProt 467–662 Author chain E； PDBConstruct 6–201； UniProt 467–662 Author chain J； PDBConstruct 6–201； UniProt 467–662

Eukaryotic peptide chain release factor subunit 1

Schizosaccharomyces pombe

UniProt P79063

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Eukaryotic peptide chain release factor GTP-binding subunit × 1 （O74718）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Eukaryotic peptide chain release factor GTP-binding subunit × 1 （O74718）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Eukaryotic peptide chain release factor GTP-binding subunit × 1 （O74718）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Eukaryotic peptide chain release factor GTP-binding subunit × 1 （O74718）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ERF1_SCHPO
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 9–441； UniProt 1–433 Author chain C； PDBConstruct 9–441； UniProt 1–433 Author chain H； PDBConstruct 9–441； UniProt 1–433 Author chain K； PDBConstruct 9–441； UniProt 1–433

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3e20
Deposition date deposition_date	2008-08-05
Structure title title	Crystal structure of S.pombe eRF1/eRF3 complex
Keywords keywords	;Sup35, Sup45, translation termination, peptide release, GTP-binding, Nucleotide-binding, Phosphoprotein, Protein biosynthesis, TRANSLATION ;; TRANSLATION
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3e20__assembly_4__model_1

Assembly 4 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3e20__assembly_4__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3e20__assembly_4__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	28.88 Å
Rg (electron density)	28.23 Å
Total Rg	28.80 Å
Atom count	2936
Residues	371
Excluded volume	52798 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3e20__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3e20__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3e20__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3e20__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Eukaryotic peptide chain release factor GTP-binding subunit
Molecular weight formula_weight	22208.7 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D,E,J
Atom count atom_count	13096

GPLGSAPFIMPIASKYKDLGTILEGKIEAGSIKKNSNVLVMPINQTLEVTAIYDEADEEISSSICGDQVRLRVRGDDSDVQTGYVLTSTKNPVHATTRFIAQIAILELPSILTTGYSCVMHIHTAVEEVSFAKLLHKLDKTNRKSKKPPMFATKGMKIIAELETQTPVCMERFEDYQYMGRFTLRDQGTTVAVGKVVKILD

Source Source

Source organism organism	Schizosaccharomyces pombe
Common name common_name	Fission yeast
NCBI taxonomy ID ncbi_taxonomy_id	4896
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Eukaryotic peptide chain release factor subunit 1
Molecular weight formula_weight	49951.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,B,H,K

MHHHHHHMMSETAEKAIEIWKIRRLVKQLINCHGNGTSMITLIIPPGEQISRYSNMLAEEYGTASNIKSRVNRLSVLSAITSTRERLKLYNKVPDNGLVIYCGEVIMEGNKTRKLNIDFEPFKPINTSQYLCDNKFHTEALAELLESDQRFGFIVMDGHQTLYGVVSGSAREVLQRFTVDLPKKHGRGGQSALRFARLRDEKRHNYVRKVAEGAVQHFITDDKPNVAGIVLAGSADFKTELGQSDLFDQRLQSRIIKTVDVSYGGDAGFNQAIELAADTLSNVKYVQEKKLIQRFFDEISLDSGKYCFGVVDTMNALQEGAVETLLCFADLDMIRYEFKNSEGNPVITYMTKEQEEKDSTNSFLLDKDTGAEMELVSSMLLSEWLAEHYKDYGANLEFVSDRSQEGMQFVKGFGGIGAVMRYQLDLSMLDPESDEFYSDSD

Source Source

Source organism organism	Schizosaccharomyces pombe
Common name common_name	Fission yeast
NCBI taxonomy ID ncbi_taxonomy_id	4896
Host organism host_organism	Escherichia coli

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6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id	3e20A01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	3e20A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	3e20B01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	960 — Translation, Eukaryotic Peptide Chain Release Factor Subunit 1; Chain A
Homologous superfamily homologous superfamily	10 — eRF1 domain 1

Domain ID domain_id	3e20B02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	30 — Ribosomal protein L30/S12

Domain ID domain_id	3e20C01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	960 — Translation, Eukaryotic Peptide Chain Release Factor Subunit 1; Chain A
Homologous superfamily homologous superfamily	10 — eRF1 domain 1

Domain ID domain_id	3e20C02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	30 — Ribosomal protein L30/S12

Domain ID domain_id	3e20D01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	3e20D02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	3e20E01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	3e20E02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	3e20H01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	2070 —

Domain ID domain_id	3e20H02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	30 — Ribosomal protein L30/S12

Domain ID domain_id	3e20J01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	3e20J02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	3e20K01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	2070 —

Domain ID domain_id	3e20K02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	30 — Ribosomal protein L30/S12

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Unit-cell length a length_a	129.848 Å
Unit-cell length b length_b	129.848 Å
Unit-cell length c length_c	332.638 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	P 43
Space-group number int_tables_number	78
Crystal system crystal_system	—

Resolution resolution	3.500 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2591
R_work r_work	0.2581
R_free r_free	0.2799

Crystal structure of S.pombe eRF1/eRF3 complex

1. Protein Identity and Related Structures Protein Identity & Related Structures

Eukaryotic peptide chain release factor GTP-binding subunit

State in the Current Structure

Other States of the Same Protein in the Database

Eukaryotic peptide chain release factor subunit 1

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3e20__assembly_4__model_1

3e20__assembly_4__model_1 | I(q)

3e20__assembly_4__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

7. Citations (1)

Crystal structure of S.pombe eRF1/eRF3 complex

1. Protein Identity and Related Structures Protein Identity & Related Structures

Eukaryotic peptide chain release factor GTP-binding subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Eukaryotic peptide chain release factor subunit 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3e20__assembly_4__model_1

3e20__assembly_4__model_1 | I(q)

3e20__assembly_4__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

7. Citations (1)